title: Effect of chain-linkage on the structure of phosphatidyl choline bilayers. Hydration studies of 1-hexadecyl 2-palmitoyl-sn-glycero-3-phosphocholine.
abstract: While hydrated dipalmitoyl phosphatidylcholine (DPPC) forms tilted chain L beta' bilayers in the gel phase, the ether-linked analogue dihexadecyl phosphatidylcholine (DHPC) exhibits gel phase polymorphism. At low hydration DHPC forms L beta' phases but at greater than 30% H2O a chain-interdigitated gel phase is observed (Ruocco, M. J., D. S. Siminovitch, and R. G. Griffin. 1985. Biochemistry. 24:2406-2411; Kim, J.T., J. Mattai, and G.G. Shipley. 1987. Biochemistry. 26:6599-6603). In this study we report the behavior of a phosphatidylcholine (PC) with both types of chain linkage, 1-hexadecyl-2-palmitoyl-sn-glycero-3-phosphocholine (HPPC). HPPC has been investigated as a function of hydration using differential scanning calorimetry (DSC) and x-ray diffraction. By DSC, over the hydration range 5. 1-70.3 wt% H2O, HPPC exhibits two reversible transitions. The reversible main chain-melting transition decreases from 69 degrees C, reaching a limiting value of 40 degrees C at full hydration. X-ray diffraction patterns of hydrated HPPC have been recorded as a function of hydration at 20 degrees and 50 degrees C. At 50 degrees C, melted-chain L alpha bilayer phases are observed at all hydrations. At 20 degrees C, at low hydrations (less than 34 wt% H2O) HPPC exhibits diffraction patterns characteristic of bilayer gel phases similar to those of the gel phase of DPPC. In contrast, at greater than or equal to 34 wt% H2O, HPPC shows a much reduced bilayer periodicity, d = 47 A, and a single sharp reflection at 4.0 A in the wide angle region. This diffraction pattern is identical to that exhibited by the interdigitated phase of DHPC. Therefore, in the gel phase HPPC undergoes a hydration-dependent conversion from a regular bilayer structure to an interdigitated bilayer arrangement. Clearly, the presence of a single ether linkage (at the sn-i position) is sufficient to allow formation of the chain-interdigitated phase in a hydration-dependent way essentially identical to that of DHPC.
authors.affiliation: Department of Biophysics, Boston University School of Medicine, Housman Medical Research Center, Massachusetts 02118-2394.
authors.forename: N S
authors.initials: NS
authors.lastname: Haas
authors.forename: P K
authors.initials: PK
authors.lastname: Sripada
authors.forename: G G
authors.initials: GG
authors.lastname: Shipley
mesh_terms: D002152:Calorimetry, Differential Scanning; D007700:Kinetics; D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D008954:Models, Biological; D008968:Molecular Conformation; D010742:Phospholipid Ethers; D013816:Thermodynamics; D014961:X-Ray Diffraction
chemical_list: D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D010742:Phospholipid Ethers; C082824:1-hexadecyl-2-palmitoyl-sn-glycero-3-phosphocholine